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首页> 外文期刊>Yeast >HIV-1 integrase trafficking in S. cerevisiae: a useful model to dissect the microtubule network involvement of viral protein nuclear import
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HIV-1 integrase trafficking in S. cerevisiae: a useful model to dissect the microtubule network involvement of viral protein nuclear import

机译：酿酒酵母中的HIV-1整合运输：剖析病毒蛋白核输入的微管网络参与的有用模型

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Intracellular transport of karyophilic cargos comprises translocation to the nuclear envelope and subsequent nuclear import. Small cargos such as isolated proteins can reach the nuclear envelope by diffusion but movement of larger structures dependson active translocation, typically using microtubules. Centripetal transport ends at the perinuclear microtubule organizing centre called the spindle pole body (SPB) in yeast. Previously, we found by two hybrids that the karyophilic lentiviral-encoded integrase (IN) interacts with two yeast microtubule-associated proteins, Dyn2p (dynein light chain protein) and Stu2p, a centrosomal protein (de Soultrait et al., 2002). Thus, to investigate the hinge between cytoplasmic retrograde transport and nuclear import, we decided to analyse HIV-1 IN trafficking in yeast as the model, since each of these biological mechanisms is evolutionarily conserved in eukaryotic cells. Here, we found an accumulation of IN at the SPB in yeast via Stu2p colocalization. Disruption of the microtubule network by nocodazole or IN expression in a dynein 2-deficient yeast strain prevented IN accumulation in the nuclear periphery and additionally inhibited IN transport into the nucleus. By mutagenesis, we showed that trafficking ofIN towards the SPB requires the C-terminus of the molecule. Taking our findings together, we proposed a model in which IN nuclear import seems to depend on an essential intermediate step in the SPB. We found that Dyn2p and Stu2p play an important role indriving IN toward MTOC and could optimize nuclear entry of the retroviral enzyme. Our results suggest a new hypothesis in keeping with the current HIV-1 intracellular trafficking model.
机译：嗜核货物的细胞内运输包括易位至核膜和随后的核输入。诸如分离的蛋白质之类的小货物可以通过扩散到达核被膜，但是较大结构的移动取决于主动易位，通常使用微管。向心转运终止于酵母中称为纺锤极体（SPB）的核周微管组织中心。以前，我们通过两个杂交体发现，嗜核慢病毒编码整合酶（IN）与两个酵母微管相关蛋白Dyn2p（动力蛋白轻链蛋白）和Stu2p（一种中心体蛋白）相互作用（de Soultrait等，2002）。因此，为了研究细胞质逆行运输和核输入之间的关系，我们决定以酵母为模型分析HIV-1 IN的运输，因为这些生物学机制中的每一个在真核细胞中都是进化保守的。在这里，我们通过Stu2p共定位在酵母中的SPB处发现了IN的积累。动力蛋白2缺陷型酵母菌株中诺考达唑或IN的表达破坏微管网络，阻止了IN在核外围的积累，并进一步抑制了IN在核中的转运。通过诱变，我们表明向SPB的IN转运需要分子的C端。综合我们的发现，我们提出了一个模型，在该模型中，IN核进口似乎取决于SPB中必不可少的中间步骤。我们发现，Dyn2p和Stu2p在将IN向MTOC的驱动中起着重要作用，并且可以优化逆转录病毒酶的核进入。我们的结果提出了与当前HIV-1细胞内贩运模型保持一致的新假设。

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